1V9S
Crystal structure of TT0130 protein from Thermus thermophilus HB8
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-12-08 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.97874, 0.97914, 0.98400, 1.00 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 116.151, 116.151, 157.643 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.24 |
| Rwork | 0.238 |
| R-free | 0.27300 |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.051 | 0.294 |
| Number of reflections | 71836 | |
| <I/σ(I)> | 15.5 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 3.3 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.5 | 295 | ammonium sulphate, sodium citrate, dioxane, pH 5.5, microbatch, temperature 295.0K |
